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Conserved domains on  [gi|2324719237|gb|UYZ52502|]
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cytochrome oxidase subunit 3, partial (mitochondrion) [Puccinia sp.]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10108868)

cytochrome c oxidase subunit 3 is one of main transmembrane subunits of cytochrome c oxidase, the last enzyme in the respiratory electron transport chain of mitochondria or bacteria located in the mitochondrial or bacterial membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-205 1.50e-100

Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


:

Pssm-ID: 238834  Cd Length: 243  Bit Score: 290.57  E-value: 1.50e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   1 VVGVISLWFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEI 80
Cdd:cd01665    34 LILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGI 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  81 PLLNTILLLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVI 160
Cdd:cd01665   114 PLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVI 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2324719237 161 IGTIFIIVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:cd01665   194 IGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFV 238
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-205 1.50e-100

Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 290.57  E-value: 1.50e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   1 VVGVISLWFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEI 80
Cdd:cd01665    34 LILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGI 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  81 PLLNTILLLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVI 160
Cdd:cd01665   114 PLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVI 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2324719237 161 IGTIFIIVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:cd01665   194 IGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFV 238
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-205 6.36e-99

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 287.38  E-value: 6.36e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   1 VVGVISLWFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEI 80
Cdd:pfam00510  47 LLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  81 PLLNTILLLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVI 160
Cdd:pfam00510 127 PLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVI 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2324719237 161 IGTIFIIVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:pfam00510 207 IGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHFVDVVWLFLYV 251
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 7-205 2.61e-94

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 275.14  E-value: 2.61e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   7 LWFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEIPLLNTI 86
Cdd:MTH00155   54 QWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTI 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  87 LLLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFI 166
Cdd:MTH00155  134 ILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFL 213

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2324719237 167 IVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00155  214 LVCLIRHLNNHFSSNHHFGFEAAAWYWHFVDVVWLFLYI 252
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
22-205 6.26e-47

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 152.70  E-value: 6.26e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  22 HTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSptvelGSQWPApGVEPLNaFEIPLLNTILLLTSASSLTYAHHA 101
Cdd:COG1845     8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLD-LPLPLINTLLLLLSSFTVALAVRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237 102 LINGNRKSCLIGFIVTLALAVTFTGFQALKY---IEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFIIVALARIISYQL 178
Cdd:COG1845    81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160

                         170       180
                  ....*....|....*....|....*..
gi 2324719237 179 TDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:COG1845   161 TPENHTGVEAAALYWHFVDVVWIFLFA 187
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 27-204 3.83e-17

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 75.66  E-value: 3.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  27 QRSLNI-GVILFIVSEIFFFVSIFWAYFhsalsptvELGSQWPAPGVEPLNAFEIPLL--NTILLLTSASSLTYAHHALI 103
Cdd:TIGR02897   6 QGRLNIlGFWIFLGAEIALFATLFATYL--------VLQHGGDYAGKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237 104 NGNRKSCLIGFIVTLALAVTFTGFQALK---YIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFIIVALARIISYQLTD 180
Cdd:TIGR02897  78 KENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTP 157

                         170       180
                  ....*....|....*....|....
gi 2324719237 181 HHHLGFEAAALYWHFVDVVWLFLF 204
Cdd:TIGR02897 158 YTAPKVFIVSLYWHFLDVVWVFIF 181
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-205 1.50e-100

Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 290.57  E-value: 1.50e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   1 VVGVISLWFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEI 80
Cdd:cd01665    34 LILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGI 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  81 PLLNTILLLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVI 160
Cdd:cd01665   114 PLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVI 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2324719237 161 IGTIFIIVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:cd01665   194 IGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFV 238
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-205 6.36e-99

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 287.38  E-value: 6.36e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   1 VVGVISLWFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEI 80
Cdd:pfam00510  47 LLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  81 PLLNTILLLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVI 160
Cdd:pfam00510 127 PLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVI 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2324719237 161 IGTIFIIVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:pfam00510 207 IGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHFVDVVWLFLYV 251
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 7-205 2.61e-94

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 275.14  E-value: 2.61e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   7 LWFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEIPLLNTI 86
Cdd:MTH00155   54 QWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTI 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  87 LLLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFI 166
Cdd:MTH00155  134 ILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFL 213

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2324719237 167 IVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00155  214 LVCLIRHLNNHFSSNHHFGFEAAAWYWHFVDVVWLFLYI 252
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 8-205 1.19e-90

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 266.43  E-value: 1.19e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   8 WFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEIPLLNTIL 87
Cdd:MTH00118   57 WWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  88 LLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFII 167
Cdd:MTH00118  137 LLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLI 216

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2324719237 168 VALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00118  217 VCLLRLIKFHFTTNHHFGFEAAAWYWHFVDVVWLFLYI 254
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-205 2.13e-90

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 265.68  E-value: 2.13e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   1 VVGVISLWFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEI 80
Cdd:MTH00189   49 LLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEV 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  81 PLLNTILLLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVI 160
Cdd:MTH00189  129 PLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVI 208

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2324719237 161 IGTIFIIVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00189  209 IGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVDVVWLFLYV 253
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 7-205 4.05e-88

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 259.82  E-value: 4.05e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   7 LWFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEIPLLNTI 86
Cdd:MTH00141   54 QWWRDIVRESTFQGFHTSKVQRGLRWGFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  87 LLLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFI 166
Cdd:MTH00141  134 VLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFL 213

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2324719237 167 IVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00141  214 LVCLVRLLLGHFSTNHHFGFEAAAWYWHFVDVVWLFLYL 252
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-205 2.17e-85

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 253.14  E-value: 2.17e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   1 VVGVISLWFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEI 80
Cdd:MTH00024   50 IVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSV 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  81 PLLNTILLLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVI 160
Cdd:MTH00024  130 PLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVI 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2324719237 161 IGTIFIIVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00024  210 IGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVDVVWLFLYL 254
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 7-205 2.52e-84

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 250.48  E-value: 2.52e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   7 LWFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEIPLLNTI 86
Cdd:MTH00052   57 VWWRDVIRESTYQGHHTLIVKQGLKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  87 LLLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFI 166
Cdd:MTH00052  137 VLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFL 216

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2324719237 167 IVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00052  217 LVCLFRLINHQFTRHHHFGFEAAAWYWHFVDVVWLFLFI 255
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 8-205 3.01e-83

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 247.72  E-value: 3.01e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   8 WFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEIPLLNTIL 87
Cdd:MTH00099   57 WWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  88 LLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFII 167
Cdd:MTH00099  137 LLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLI 216

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2324719237 168 VALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00099  217 VCFLRQLKFHFTSNHHFGFEAAAWYWHFVDVVWLFLYV 254
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 4-205 4.81e-81

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 241.94  E-value: 4.81e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   4 VISLWFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEIPLL 83
Cdd:MTH00039   52 TSINWWRDVIREATFQGMHTLIVINGLRYGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  84 NTILLLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGT 163
Cdd:MTH00039  132 NTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGT 211

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2324719237 164 IFIIVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00039  212 TFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVDVVWLFLYV 253
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 8-205 1.51e-80

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 240.82  E-value: 1.51e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   8 WFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEIPLLNTIL 87
Cdd:MTH00130   57 WWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  88 LLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFII 167
Cdd:MTH00130  137 LLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLA 216

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2324719237 168 VALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00130  217 VCLLRQIQYHFTSEHHFGFEAAAWYWHFVDVVWLFLYI 254
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 8-205 3.50e-80

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 239.65  E-value: 3.50e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   8 WFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEIPLLNTIL 87
Cdd:MTH00075   57 WWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  88 LLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFII 167
Cdd:MTH00075  137 LLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLL 216

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2324719237 168 VALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00075  217 VCLLRQINFHFTSQHHFGFEAAAWYWHFVDVVWLFLYV 254
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 8-205 1.23e-77

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 233.53  E-value: 1.23e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   8 WFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEIPLLNTIL 87
Cdd:MTH00219   58 WWRDVIRESTFMGLHTSKVSTGLRIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAV 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  88 LLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFII 167
Cdd:MTH00219  138 LLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLF 217

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2324719237 168 VALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00219  218 VCFMRGLMLHFSKNHHFGFEAAAWYWHFVDVVWLFLYV 255
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 8-205 1.22e-70

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 215.47  E-value: 1.22e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   8 WFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEIPLLNTIL 87
Cdd:MTH00009   55 WWRDVIREGTYMGHHTSYVTKGLRWGMILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAV 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  88 LLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFII 167
Cdd:MTH00009  135 LLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLF 214

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2324719237 168 VALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00009  215 VCLLRTWSHHFSTGHHFGFEAAAWYWHFVDVVWIFLYL 252
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 6-205 1.01e-67

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 209.54  E-value: 1.01e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   6 SLWFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEIPLLNT 85
Cdd:MTH00028   55 SAWWRDVIREGTHQGHHTQIVVRGLKLGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNT 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  86 ILLLTSASSLTYAHHALINGN------------------------------------RKSCLIGFIVTLALAVTFTGFQA 129
Cdd:MTH00028  135 TILLSSGATVTWAHHAIIGTGnpaslekgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQA 214

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2324719237 130 LKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFIIVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00028  215 FEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYV 290
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 4-205 1.96e-65

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 202.11  E-value: 1.96e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   4 VISLWFRDVSAEGaLGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEIPLL 83
Cdd:MTH00083   50 ISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  84 NTILLLTSASSLTYAHHALINGNrKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGT 163
Cdd:MTH00083  129 NTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGG 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2324719237 164 IFIIVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:MTH00083  208 LFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDVVWLFLFV 249
PLN02194 PLN02194
cytochrome-c oxidase
 7-205 5.57e-63

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 196.04  E-value: 5.57e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237   7 LWFRDVSAEGALGGYHTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFEIPLLNTI 86
Cdd:PLN02194   59 VWWRDVLRESTLEGHHTKVVQLGPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTP 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  87 LLLTSASSLTYAHHALINGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFI 166
Cdd:PLN02194  139 ILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFL 218

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2324719237 167 IVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:PLN02194  219 IICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFV 257
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 22-205 1.51e-62

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


Pssm-ID: 238227  Cd Length: 183  Bit Score: 192.03  E-value: 1.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  22 HTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSPTVELGsqwpapgvEPLNAFEIPLLNTILLLTSASSLTYAHHA 101
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237 102 LI--NGNRKSCLIGFIVTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFIIVALARIISYQLT 179
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180
                  ....*....|....*....|....*.
gi 2324719237 180 DHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFP 178
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
22-205 6.26e-47

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 152.70  E-value: 6.26e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  22 HTFDVQRSLNIGVILFIVSEIFFFVSIFWAYFHSALSptvelGSQWPApGVEPLNaFEIPLLNTILLLTSASSLTYAHHA 101
Cdd:COG1845     8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLD-LPLPLINTLLLLLSSFTVALAVRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237 102 LINGNRKSCLIGFIVTLALAVTFTGFQALKY---IEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFIIVALARIISYQL 178
Cdd:COG1845    81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160

                         170       180
                  ....*....|....*....|....*..
gi 2324719237 179 TDHHHLGFEAAALYWHFVDVVWLFLFI 205
Cdd:COG1845   161 TPENHTGVEAAALYWHFVDVVWIFLFA 187
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 31-204 3.24e-24

NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.


Pssm-ID: 239213  Cd Length: 186  Bit Score: 94.22  E-value: 3.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  31 NIGVILFIVSEIFFFVSIFWAYF-HSALSPTV-ELGSQWPAPGveplnafeIPLLNTILLLTSASSLTYAHHALINGNRK 108
Cdd:cd02862    10 KLGMWVFILSELLAFGALFIAYAvYRALYPELfAAGSAHLDLL--------LGALNTLVLLTSSFTVALAVRAARAGRRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237 109 SCLIGFIVTLALAVTFTGFQALKY---IEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFIIVALARIISYQLTDHHHLG 185
Cdd:cd02862    82 RARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLHVLIGLGILLWVAWRARRGRYSARDYEG 161

                         170
                  ....*....|....*....
gi 2324719237 186 FEAAALYWHFVDVVWLFLF 204
Cdd:cd02862   162 VEAAALYWHMVDLVWIVLF 180
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 36-204 3.07e-22

Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.


Pssm-ID: 239214  Cd Length: 186  Bit Score: 88.84  E-value: 3.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  36 LFIVSEIFFFVSIFWAYFhsALSPTVelgsqwpAPGVEPLNAFEIPL--LNTILLLTSASSLTYAHHALINGNRKSCLIG 113
Cdd:cd02863    15 IYLMSDCILFATLFATYA--VLSGNT-------AGGPPGHELFELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILW 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237 114 FIVTLALAVTFTGFQALK---YIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFIIVALARIISYQLTDHHHLGFEAAA 190
Cdd:cd02863    86 LIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLS 165

                         170
                  ....*....|....
gi 2324719237 191 LYWHFVDVVWLFLF 204
Cdd:cd02863   166 LFWHFLDIVWIFVF 179
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 36-204 5.50e-19

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239215  Cd Length: 202  Bit Score: 81.01  E-value: 5.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  36 LFIVSEIFFFVSIFWAYFHSALSPTVelgsQWPAPG---VEPLNAFEIPL----LNTILLLTSASSLTYAHHALINGNRK 108
Cdd:cd02864    15 FFLLSDAFIFSSFLIAYMTARISTTE----PWPLPSdvfALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237 109 SCLIGFIVTLALAVTFTGFQALKYIEAPFTISDG---------VFGSTFFFSTGFHGIHVIIGTIFIIVALARIISYQLT 179
Cdd:cd02864    91 AAARLMLATALLGATFVGMQAFEWTKLIVEEGVRpwgnpwgaaQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQ 170

                         170       180
                  ....*....|....*....|....*.
gi 2324719237 180 DH-HHLGFEAAALYWHFVDVVWLFLF 204
Cdd:cd02864   171 RIgRYEIVEIAGLYWHFVDLVWVFIF 196
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 32-204 5.72e-18

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239216  Cd Length: 184  Bit Score: 77.80  E-value: 5.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  32 IGVILFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVeplnafeiPLLNTILLLTSASSLTYAHHALINGNRKSCL 111
Cdd:cd02865    11 WGLWVFMAVEGTLFALLISAYFMRMTSGDWQPGAPLPLPNL--------LSLNTAVLAASSVAMQWARRAARRNRRVLAR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237 112 IGFIVTLALAVTFTGFQALKYIEAPF---TISDGVFGSTFFFSTGFHGIHVIIGTIFIIVALARIISYQLTDHHHLGFEA 188
Cdd:cd02865    83 LGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVEL 162

                         170
                  ....*....|....*.
gi 2324719237 189 AALYWHFVDVVWLFLF 204
Cdd:cd02865   163 CALYWHFLLLVWLVLL 178
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 27-204 3.83e-17

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 75.66  E-value: 3.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  27 QRSLNI-GVILFIVSEIFFFVSIFWAYFhsalsptvELGSQWPAPGVEPLNAFEIPLL--NTILLLTSASSLTYAHHALI 103
Cdd:TIGR02897   6 QGRLNIlGFWIFLGAEIALFATLFATYL--------VLQHGGDYAGKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237 104 NGNRKSCLIGFIVTLALAVTFTGFQALK---YIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIFIIVALARIISYQLTD 180
Cdd:TIGR02897  78 KENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTP 157

                         170       180
                  ....*....|....*....|....
gi 2324719237 181 HHHLGFEAAALYWHFVDVVWLFLF 204
Cdd:TIGR02897 158 YTAPKVFIVSLYWHFLDVVWVFIF 181
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 36-205 3.96e-10

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 57.23  E-value: 3.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  36 LFIVSEIFFFVSIFWAYFHSALSPTVELGSqwpapgveplnAFEIPLLNTILLLTSASSLTYAHHALingNRKSCLIGFI 115
Cdd:MTH00049   59 LFILSEVIIFGSLLVCCLWFDDWSYISLSS-----------SLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLY 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237 116 VTLALAVTFTGFQALKYIEAPFTISDGVFGSTFFFSTGFHGIHVIIGTIfiivALARIISYQLTDHHHLGFEAAALYWHF 195
Cdd:MTH00049  125 LTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVV----GLSTLLLVGSSSFGVYRSTVLTWYWHF 200

                         170
                  ....*....|
gi 2324719237 196 VDVVWLFLFI 205
Cdd:MTH00049  201 VDYIWLLVYL 210
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 78-204 2.16e-09

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 54.79  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324719237  78 FEIP--LLNTILLLTSasSLTYAHHAL-INGNRKSCLIGFivtlaLAVTF---TGFQALKYIEAPFTISDGV------FG 145
Cdd:PRK10663   64 FELPfvLVETFLLLFS--SITYGMAAIaMYKNNKSQVISW-----LALTFlfgAGFIGMEIYEFHHLIVEGMgpdrsgFL 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2324719237 146 STFFFSTGFHGIHVIIGTIFIIVALARIISYQLTDHHHLGFEAAALYWHFVDVVWLFLF 204
Cdd:PRK10663  137 SAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVF 195
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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